Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Dipeptidyl peptidase 4 (EC 3.4.14.5) (ADABP) (Adenosine deaminase complexing protein 2) (ADCP-2) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (TP103) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]

 DPP4_HUMAN              Reviewed;         766 AA.
P27487; Q53TN1;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
07-JUN-2017, entry version 196.
RecName: Full=Dipeptidyl peptidase 4;
EC=3.4.14.5 {ECO:0000269|PubMed:10593948};
AltName: Full=ADABP;
AltName: Full=Adenosine deaminase complexing protein 2;
Short=ADCP-2;
AltName: Full=Dipeptidyl peptidase IV;
Short=DPP IV;
AltName: Full=T-cell activation antigen CD26;
AltName: Full=TP103;
AltName: CD_antigen=CD26;
Contains:
RecName: Full=Dipeptidyl peptidase 4 membrane form;
AltName: Full=Dipeptidyl peptidase IV membrane form;
Contains:
RecName: Full=Dipeptidyl peptidase 4 soluble form;
AltName: Full=Dipeptidyl peptidase IV soluble form;
Name=DPP4; Synonyms=ADCP2, CD26;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1352704; DOI=10.1016/0167-4781(92)90036-Y;
Misumi Y., Hayashi Y., Arakawa F., Ikehara Y.;
"Molecular cloning and sequence analysis of human dipeptidyl peptidase
IV, a serine proteinase on the cell surface.";
Biochim. Biophys. Acta 1131:333-336(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Colon;
PubMed=1347043;
Darmoul D., Lacasa M., Baricault L., Marguet D., Sapin C., Trotot P.,
Barbat A.;
"Dipeptidyl peptidase IV (CD 26) gene expression in enterocyte-like
colon cancer cell lines HT-29 and Caco-2. Cloning of the complete
human coding sequence and changes of dipeptidyl peptidase IV mRNA
levels during cell differentiation.";
J. Biol. Chem. 267:4824-4833(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peripheral blood;
PubMed=1352530;
Tanaka T., Camerini D., Seed B., Torimoto Y., Dang N.H., Kameoka J.,
Dahlberg H.N., Schlossman S.F., Morimoto C.;
"Cloning and functional expression of the T cell activation antigen
CD26.";
J. Immunol. 149:481-486(1992).
[4]
ERRATUM.
PubMed=8094732;
Tanaka T.;
J. Immunol. 150:2090-2090(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=7927537; DOI=10.1007/BF01246674;
Abbott C.A., Baker E., Sutherland G.R., McCaughan G.W.;
"Genomic organization, exact localization, and tissue expression of
the human CD26 (dipeptidyl peptidase IV) gene.";
Immunogenetics 40:331-338(1994).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 545-766.
TISSUE=Colon;
PubMed=1977364; DOI=10.1111/j.1469-1809.1990.tb00377.x;
Darmoul D., Lacasa M., Chantret I., Swallow D., Trugnan G.;
"Isolation of a cDNA probe for the human intestinal
dipeptidylpeptidase IV and assignment of the gene locus DPP4 to
chromosome 2.";
Ann. Hum. Genet. 54:191-197(1990).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
PubMed=7487939; DOI=10.1042/bj3110835;
Boehm S.K., Gum J.R. Jr., Erickson R.H., Hicks J.W., Kim Y.S.;
"Human dipeptidyl peptidase IV gene promoter: tissue-specific
regulation from a TATA-less GC-rich sequence characteristic of a
housekeeping gene promoter.";
Biochem. J. 311:835-843(1995).
[12]
PROTEIN SEQUENCE OF 1-22, AND TISSUE SPECIFICITY.
PubMed=1677636;
Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J.,
Maroux S.;
"Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human
small intestine and colon.";
Gastroenterology 101:618-625(1991).
[13]
PROTEIN SEQUENCE OF 29-34 AND 39-43, FUNCTION, INTERACTION WITH ADA,
AND SUBCELLULAR LOCATION.
PubMed=10951221; DOI=10.1046/j.1432-1327.2000.01634.x;
Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R.,
Haemers A., Scharpe S., De Meester I.;
"Molecular characterization of dipeptidyl peptidase activity in serum:
soluble CD26/dipeptidyl peptidase IV is responsible for the release of
X-Pro dipeptides.";
Eur. J. Biochem. 267:5608-5613(2000).
[14]
PROTEIN SEQUENCE OF 659-669, FUNCTION, ENZYME REGULATION, INTERACTION
WITH GPC3, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17549790; DOI=10.1002/pmic.200600654;
Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.;
"The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and
inhibits the dipeptidyl peptidase activity of CD26.";
Proteomics 7:2300-2310(2007).
[15]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Kidney;
PubMed=8096237; DOI=10.1084/jem.177.4.1135;
Morrison M.E., Vijayasaradhi S., Engelstein D., Albino A.P.,
Houghton A.N.;
"A marker for neoplastic progression of human melanocytes is a cell
surface ectopeptidase.";
J. Exp. Med. 177:1135-1143(1993).
[16]
INTERACTION WITH ADA, AND SUBCELLULAR LOCATION.
PubMed=8101391; DOI=10.1126/science.8101391;
Kameoka J., Tanaka T., Nojima Y., Schlossman S.F., Morimoto C.;
"Direct association of adenosine deaminase with a T cell activation
antigen, CD26.";
Science 261:466-469(1993).
[17]
INTERACTION WITH ADA.
PubMed=7907293; DOI=10.1002/eji.1830240311;
De Meester I., Vanham G., Kestens L., Vanhoof G., Bosmans E.,
Gigase P., Scharpe S.;
"Binding of adenosine deaminase to the lymphocyte surface via CD26.";
Eur. J. Immunol. 24:566-570(1994).
[18]
ASSOCIATION WITH COLLAGEN.
PubMed=8526932; DOI=10.1006/bbrc.1995.2782;
Loster K., Zeilinger K., Schuppan D., Reutter W.;
"The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the
collagen-binding site.";
Biochem. Biophys. Res. Commun. 217:341-348(1995).
[19]
INDUCTION.
PubMed=9413751;
Cordero O.J., Salgado F.J., Vinuela J.E., Nogueira M.;
"Interleukin-12 enhances CD26 expression and dipeptidyl peptidase IV
function on human activated lymphocytes.";
Immunobiology 197:522-533(1997).
[20]
FUNCTION, AND MUTAGENESIS OF GLU-205 AND GLU-206.
PubMed=10570924; DOI=10.1016/S0014-5793(99)01166-7;
Abbott C.A., McCaughan G.W., Gorrell M.D.;
"Two highly conserved glutamic acid residues in the predicted beta
propeller domain of dipeptidyl peptidase IV are required for its
enzyme activity.";
FEBS Lett. 458:278-284(1999).
[21]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10593948; DOI=10.1074/jbc.274.51.36505;
Park J.E., Lenter M.C., Zimmermann R.N., Garin-Chesa P., Old L.J.,
Rettig W.J.;
"Fibroblast activation protein, a dual specificity serine protease
expressed in reactive human tumor stromal fibroblasts.";
J. Biol. Chem. 274:36505-36512(1999).
[22]
ASSOCIATION WITH CANCER.
PubMed=11027426; DOI=10.1054/bjoc.2000.1410;
Cordero O.J., Ayude D., Nogueira M., Rodriguez-Berrocal F.J.,
de la Cadena M.P.;
"Preoperative serum CD26 levels: diagnostic efficiency and predictive
value for colorectal cancer.";
Br. J. Cancer 83:1139-1146(2000).
[23]
INDUCTION.
PubMed=10880264; DOI=10.1006/cyto.1999.0643;
Salgado F.J., Vela E., Martin M., Franco R., Nogueira M.,
Cordero O.J.;
"Mechanisms of CD26/dipeptidyl peptidase IV cytokine-dependent
regulation on human activated lymphocytes.";
Cytokine 12:1136-1141(2000).
[24]
FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, AND
SUBCELLULAR LOCATION.
PubMed=10900005; DOI=10.1073/pnas.97.15.8439;
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H.,
Schlossman S.F., Morimoto C.;
"Internalization of CD26 by mannose 6-phosphate/insulin-like growth
factor II receptor contributes to T cell activation.";
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000).
[25]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11772392; DOI=10.1042/0264-6021:3610203;
Gines S., Marino M., Mallol J., Canela E.I., Morimoto C.,
Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.;
"Regulation of epithelial and lymphocyte cell adhesion by adenosine
deaminase-CD26 interaction.";
Biochem. J. 361:203-209(2002).
[26]
GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=11773049; DOI=10.1074/jbc.M109357200;
Alfalah M., Jacob R., Naim H.Y.;
"Intestinal dipeptidyl peptidase IV is efficiently sorted to the
apical membrane through the concerted action of N- and O-glycans as
well as association with lipid microdomains.";
J. Biol. Chem. 277:10683-10690(2002).
[27]
INTERACTION WITH PTPRC, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=12676959; DOI=10.1074/jbc.M212978200;
Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R.,
Cordero O.J., Nogueira M.;
"A role for interleukin-12 in the regulation of T cell plasma membrane
compartmentation.";
J. Biol. Chem. 278:24849-24857(2003).
[28]
INTERACTION WITH ADA.
PubMed=15016824; DOI=10.1074/jbc.M401023200;
Gonzalez-Gronow M., Hershfield M.S., Arredondo-Vega F.X., Pizzo S.V.;
"Cell surface adenosine deaminase binds and stimulates plasminogen
activation on 1-LN human prostate cancer cells.";
J. Biol. Chem. 279:20993-20998(2004).
[29]
HOMODIMERIZATION, AND MUTAGENESIS OF HIS-750.
PubMed=15448155; DOI=10.1074/jbc.M406185200;
Chien C.H., Huang L.H., Chou C.Y., Chen Y.S., Han Y.S., Chang G.G.,
Liang P.H., Chen X.;
"One site mutation disrupts dimer formation in human DPP-IV
proteins.";
J. Biol. Chem. 279:52338-52345(2004).
[30]
FUNCTION, INTERACTION WITH ADA, AND MUTAGENESIS OF ASN-85; ASN-92;
ASN-150; ASN-219; ASN-229; ASN-281; ASN-321; ASN-520 AND ASN-685.
PubMed=14691230; DOI=10.1110/ps.03352504;
Aertgeerts K., Ye S., Shi L., Prasad S.G., Witmer D., Chi E.,
Sang B.C., Wijnands R.A., Webb D.R., Swanson R.V.;
"N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on
enzyme activity, homodimer formation, and adenosine deaminase
binding.";
Protein Sci. 13:145-154(2004).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-520 AND ASN-685.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[32]
INDUCTION BY HYPOXIA.
PubMed=16670267; DOI=10.1182/blood-2006-02-001016;
Eltzschig H.K., Faigle M., Knapp S., Karhausen J., Ibla J.,
Rosenberger P., Odegard K.C., Laussen P.C., Thompson L.F.,
Colgan S.P.;
"Endothelial catabolism of extracellular adenosine during hypoxia: the
role of surface adenosine deaminase and CD26.";
Blood 108:1602-1610(2006).
[33]
FUNCTION, HETERODIMERIZATION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=16651416; DOI=10.1158/0008-5472.CAN-05-1245;
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.;
"The protease complex consisting of dipeptidyl peptidase IV and
seprase plays a role in the migration and invasion of human
endothelial cells in collagenous matrices.";
Cancer Res. 66:4652-4661(2006).
[34]
FUNCTION, IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, HOMODIMERIZATION,
INTERACTION WITH CARD11 AND CAV1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF HIS-750.
PubMed=17287217; DOI=10.1074/jbc.M609157200;
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O.,
Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.;
"Caveolin-1 triggers T-cell activation via CD26 in association with
CARMA1.";
J. Biol. Chem. 282:10117-10131(2007).
[35]
FUNCTION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
PubMed=18708048; DOI=10.1016/j.yexcr.2008.07.024;
Shin J.W., Jurisic G., Detmar M.;
"Lymphatic-specific expression of dipeptidyl peptidase IV and its dual
role in lymphatic endothelial function.";
Exp. Cell Res. 314:3048-3056(2008).
[36]
REVIEW.
PubMed=19557413; DOI=10.1007/s00262-009-0728-1;
Cordero O.J., Salgado F.J., Nogueira M.;
"On the origin of serum CD26 and its altered concentration in cancer
patients.";
Cancer Immunol. Immunother. 58:1723-1747(2009).
[37]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-92; ASN-150; ASN-520 AND
ASN-685.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[39]
INTERACTION WITH HUMAN CORONAVIRUS-EMC SPIKE PROTEIN.
PubMed=23486063; DOI=10.1038/nature12005;
Raj V.S., Mou H., Smits S.L., Dekkers D.H., Muller M.A., Dijkman R.,
Muth D., Demmers J.A., Zaki A., Fouchier R.A., Thiel V., Drosten C.,
Rottier P.J., Osterhaus A.D., Bosch B.J., Haagmans B.L.;
"Dipeptidyl peptidase 4 is a functional receptor for the emerging
human coronavirus-EMC.";
Nature 495:251-254(2013).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[41]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-766 IN COMPLEX WITH
INHIBITOR, AND HOMODIMERIZATION.
PubMed=12832764; DOI=10.1107/S0907444903010059;
Oefner C., D'Arcy A., Mac Sweeney A., Pierau S., Gardiner R.,
Dale G.E.;
"High-resolution structure of human apo dipeptidyl peptidase IV/CD26
and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-
acetyl]-2-cyano-(S)-pyrrolidine.";
Acta Crystallogr. D 59:1206-1212(2003).
[42]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION,
GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, AND
DISULFIDE BONDS.
PubMed=12646248; DOI=10.1016/S0006-291X(03)00258-4;
Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H.,
Sugiyama S., Inaka K., Yamamoto A., Shimizu R.;
"The structure and function of human dipeptidyl peptidase IV,
possessing a unique eight-bladed beta-propeller fold.";
Biochem. Biophys. Res. Commun. 302:849-854(2003).
[43]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION,
GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321
AND ASN-520, AND DISULFIDE BONDS.
PubMed=12483204; DOI=10.1038/nsb882;
Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N.;
"Crystal structure of human dipeptidyl peptidase IV/CD26 in complex
with a substrate analog.";
Nat. Struct. Biol. 10:19-25(2003).
[44]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION,
GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, AND DISULFIDE
BONDS.
PubMed=12906826; DOI=10.1016/S0969-2126(03)00160-6;
Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M.;
"Structural basis of proline-specific exopeptidase activity as
observed in human dipeptidyl peptidase-IV.";
Structure 11:947-959(2003).
[45]
X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 39-766, AND GLYCOSYLATION AT
ASN-85; ASN-92; ASN-150; ASN-219; ASN-229 AND ASN-520.
PubMed=20684603; DOI=10.1021/jm100634a;
Meng W., Brigance R.P., Chao H.J., Fura A., Harrity T.,
Marcinkeviciene J., O'Connor S.P., Tamura J.K., Xie D., Zhang Y.,
Klei H.E., Kish K., Weigelt C.A., Turdi H., Wang A., Zahler R.,
Kirby M.S., Hamann L.G.;
"Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-
methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective
dipeptidyl peptidase-4 (DPP4) inhibitors.";
J. Med. Chem. 53:5620-5628(2010).
-!- FUNCTION: Cell surface glycoprotein receptor involved in the
costimulatory signal essential for T-cell receptor (TCR)-mediated
T-cell activation. Acts as a positive regulator of T-cell
coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its
binding to CAV1 and CARD11 induces T-cell proliferation and NF-
kappa-B activation in a T-cell receptor/CD3-dependent manner. Its
interaction with ADA also regulates lymphocyte-epithelial cell
adhesion. In association with FAP is involved in the pericellular
proteolysis of the extracellular matrix (ECM), the migration and
invasion of endothelial cells into the ECM. May be involved in the
promotion of lymphatic endothelial cells adhesion, migration and
tube formation. When overexpressed, enhanced cell proliferation, a
process inhibited by GPC3. Acts also as a serine exopeptidase with
a dipeptidyl peptidase activity that regulates various
physiological processes by cleaving peptides in the circulation,
including many chemokines, mitogenic growth factors, neuropeptides
and peptide hormones. Removes N-terminal dipeptides sequentially
from polypeptides having unsubstituted N-termini provided that the
penultimate residue is proline. {ECO:0000269|PubMed:10570924,
ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10900005,
ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:11772392,
ECO:0000269|PubMed:14691230, ECO:0000269|PubMed:16651416,
ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17549790,
ECO:0000269|PubMed:18708048}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided
Zaa is neither Pro nor hydroxyproline. {ECO:0000255|PROSITE-
ProRule:PRU10084, ECO:0000269|PubMed:10593948}.
-!- ENZYME REGULATION: Inhibited by GPC3 and diprotin A.
{ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:18708048}.
-!- SUBUNIT: Monomer. Homodimer (PubMed:12832764, PubMed:15448155,
PubMed:17287217, PubMed:12646248, PubMed:12483204,
PubMed:12906826). Heterodimer with Seprase (FAP)
(PubMed:16651416). Requires homodimerization for optimal
dipeptidyl peptidase activity and T-cell costimulation. Found in a
membrane raft complex, at least composed of BCL10, CARD11, DPP4
and IKBKB (PubMed:17287217). Associates with collagen
(PubMed:8526932). Interacts with PTPRC; the interaction is
enhanced in a interleukin-12-dependent manner in activated
lymphocytes (PubMed:12676959). Interacts (via extracellular
domain) with ADA; does not inhibit its dipeptidyl peptidase
activity (PubMed:15016824, PubMed:10951221, PubMed:14691230,
PubMed:7907293, PubMed:8101391). Interacts with CAV1 (via the N-
terminus); the interaction is direct (PubMed:17287217). Interacts
(via cytoplasmic tail) with CARD11 (via PDZ domain); its
homodimerization is necessary for interaction with CARD11
(PubMed:17287217). Interacts with IGF2R; the interaction is direct
(PubMed:10900005). Interacts with GPC3 (PubMed:17549790).
Interacts with human coronavirus-EMC spike protein and acts as a
receptor for this virus (PubMed:23486063).
{ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221,
ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248,
ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:12832764,
ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:14691230,
ECO:0000269|PubMed:15016824, ECO:0000269|PubMed:15448155,
ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217,
ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:23486063,
ECO:0000269|PubMed:7907293, ECO:0000269|PubMed:8101391,
ECO:0000269|PubMed:8526932}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-2871277, EBI-2871277;
P56658:ADA (xeno); NbExp=5; IntAct=EBI-2871277, EBI-7475530;
P51671:CCL11; NbExp=2; IntAct=EBI-2871277, EBI-727357;
P02778:CXCL10; NbExp=2; IntAct=EBI-2871277, EBI-7815386;
O14625:CXCL11; NbExp=2; IntAct=EBI-2871277, EBI-2871971;
P19875:CXCL2; NbExp=2; IntAct=EBI-2871277, EBI-2114901;
Q07325:CXCL9; NbExp=2; IntAct=EBI-2871277, EBI-3911467;
P01275:GCG; NbExp=4; IntAct=EBI-2871277, EBI-7629173;
P01282:VIP; NbExp=2; IntAct=EBI-2871277, EBI-751454;
-!- SUBCELLULAR LOCATION: Dipeptidyl peptidase 4 soluble form:
Secreted {ECO:0000269|PubMed:10951221}. Note=Detected in the serum
and the seminal fluid.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10900005,
ECO:0000269|PubMed:11772392, ECO:0000305|PubMed:8101391}; Single-
pass type II membrane protein. Apical cell membrane
{ECO:0000269|PubMed:11773049}; Single-pass type II membrane
protein. Cell projection, invadopodium membrane
{ECO:0000269|PubMed:16651416}; Single-pass type II membrane
protein. Cell projection, lamellipodium membrane
{ECO:0000269|PubMed:16651416}; Single-pass type II membrane
protein. Cell junction {ECO:0000269|PubMed:11772392}. Membrane
raft {ECO:0000269|PubMed:17287217}. Note=Translocated to the
apical membrane through the concerted action of N- and O-Glycans
and its association with lipid microdomains containing cholesterol
and sphingolipids (PubMed:11773049). Redistributed to membrane
rafts in T-cell in a interleukin-12-dependent activation
(PubMed:12676959). Its interaction with CAV1 is necessary for its
translocation to membrane rafts (PubMed:17287217). Colocalized
with PTPRC in membrane rafts (PubMed:12676959). Colocalized with
FAP in invadopodia and lamellipodia of migratory activated
endothelial cells in collagenous matrix. Colocalized with FAP on
endothelial cells of capillary-like microvessels but not large
vessels within invasive breast ductal carcinoma (PubMed:16651416).
Colocalized with ADA at the cell junction in lymphocyte-epithelial
cell adhesion (PubMed:11772392). Colocalized with IGF2R in
internalized cytoplasmic vesicles adjacent to the cell surface
(PubMed:10900005). {ECO:0000269|PubMed:10900005,
ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:11773049,
ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:16651416,
ECO:0000269|PubMed:17287217}.
-!- TISSUE SPECIFICITY: Expressed specifically in lymphatic vessels
but not in blood vessels in the skin, small intestine, esophagus,
ovary, breast and prostate glands. Not detected in lymphatic
vessels in the lung, kidney, uterus, liver and stomach (at protein
level). Expressed in the poorly differentiated crypt cells of the
small intestine as well as in the mature villous cells. Expressed
at very low levels in the colon. {ECO:0000269|PubMed:1677636,
ECO:0000269|PubMed:18708048}.
-!- INDUCTION: Up-regulated by IL12/interleukin-12 on activated T-
cells. IL12-activated cells expressed enhanced levels of DPP4 but
not mRNAs. Down-regulated by TNF. Up-regulated in migratory
endothelial cells and in the invasive endothelial cells in tumors.
Induced by hypoxia (PubMed:16670267).
{ECO:0000269|PubMed:10880264, ECO:0000269|PubMed:12676959,
ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:16670267,
ECO:0000269|PubMed:9413751}.
-!- DOMAIN: The extracellular cysteine-rich region is necessary for
association with collagen, dimer formation and optimal dipeptidyl
peptidase activity.
-!- PTM: The soluble form (Dipeptidyl peptidase 4 soluble form also
named SDPP) derives from the membrane form (Dipeptidyl peptidase 4
membrane form also named MDPP) by proteolytic processing.
-!- PTM: N- and O-Glycosylated. {ECO:0000269|PubMed:10900005,
ECO:0000269|PubMed:11773049, ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20684603}.
-!- PTM: Phosphorylated. Mannose 6-phosphate residues in the
carbohydrate moiety are necessary for interaction with IGF2R in
activated T-cells. Mannose 6-phosphorylation is induced during T-
cell activation. {ECO:0000269|PubMed:10900005}.
-!- MISCELLANEOUS: Level of plasma concentrations of the soluble form
(SDPP) can be managed as a colon carcinoma diagnostic and
prognostic marker.
-!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Dipeptidyl peptidase-4 entry;
URL="https://en.wikipedia.org/wiki/Dipeptidyl_peptidase-4";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DPP4ID40360ch2q24.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X60708; CAA43118.1; -; mRNA.
EMBL; M80536; AAA52308.1; -; mRNA.
EMBL; M74777; AAA51943.1; -; mRNA.
EMBL; U13735; AAB60646.1; -; Genomic_DNA.
EMBL; U13710; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13711; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13712; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13713; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13714; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13715; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13716; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13717; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13718; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13719; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13720; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13721; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13722; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13723; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13724; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13725; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13726; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13727; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13728; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13729; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13730; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13731; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13732; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13733; AAB60646.1; JOINED; Genomic_DNA.
EMBL; U13734; AAB60646.1; JOINED; Genomic_DNA.
EMBL; AB451339; BAG70153.1; -; mRNA.
EMBL; AB451488; BAG70302.1; -; mRNA.
EMBL; AC008063; AAX93179.1; -; Genomic_DNA.
EMBL; CH471058; EAX11361.1; -; Genomic_DNA.
EMBL; BC013329; AAH13329.2; -; mRNA.
EMBL; BC065265; AAH65265.1; -; mRNA.
EMBL; S79876; AAB35614.1; -; Genomic_DNA.
CCDS; CCDS2216.1; -.
PIR; S24313; CDHU26.
RefSeq; NP_001926.2; NM_001935.3.
UniGene; Hs.368912; -.
PDB; 1J2E; X-ray; 2.60 A; A/B=33-766.
PDB; 1N1M; X-ray; 2.50 A; A/B=39-766.
PDB; 1NU6; X-ray; 2.10 A; A/B=39-766.
PDB; 1NU8; X-ray; 2.50 A; A/B=39-766.
PDB; 1PFQ; X-ray; 1.90 A; A/B=36-766.
PDB; 1R9M; X-ray; 2.10 A; A/B/C/D=39-766.
PDB; 1R9N; X-ray; 2.30 A; A/B/C/D=39-766.
PDB; 1RWQ; X-ray; 2.20 A; A/B=39-766.
PDB; 1TK3; X-ray; 2.00 A; A/B=39-766.
PDB; 1TKR; X-ray; 2.70 A; A/B=39-766.
PDB; 1U8E; X-ray; 2.20 A; A/B=39-766.
PDB; 1W1I; X-ray; 3.03 A; A/B/C/D=39-766.
PDB; 1WCY; X-ray; 2.20 A; A/B=33-766.
PDB; 1X70; X-ray; 2.10 A; A/B=39-766.
PDB; 2AJL; X-ray; 2.50 A; I/J=39-766.
PDB; 2BGN; X-ray; 3.15 A; A/B/C/D=39-766.
PDB; 2BGR; X-ray; 2.00 A; A/B=29-766.
PDB; 2BUB; X-ray; 2.66 A; A/B=39-766.
PDB; 2FJP; X-ray; 2.40 A; A/B=39-766.
PDB; 2G5P; X-ray; 2.40 A; A/B=39-764.
PDB; 2G5T; X-ray; 2.30 A; A/B=39-764.
PDB; 2G63; X-ray; 2.00 A; A/B/C/D=39-764.
PDB; 2HHA; X-ray; 2.35 A; A/B=40-766.
PDB; 2I03; X-ray; 2.40 A; A/B/C/D=39-764.
PDB; 2I78; X-ray; 2.50 A; A/B/C/D=39-764.
PDB; 2IIT; X-ray; 2.35 A; A/B=39-766.
PDB; 2IIV; X-ray; 2.15 A; A/B=39-766.
PDB; 2JID; X-ray; 2.80 A; A/B=31-766.
PDB; 2OAG; X-ray; 2.30 A; A/B/C/D=39-764.
PDB; 2OGZ; X-ray; 2.10 A; A/B=39-766.
PDB; 2OLE; X-ray; 2.40 A; A/B=39-766.
PDB; 2ONC; X-ray; 2.55 A; A/B/C/D=41-766.
PDB; 2OPH; X-ray; 2.40 A; A/B=39-766.
PDB; 2OQI; X-ray; 2.80 A; A/B/C/D=39-766.
PDB; 2OQV; X-ray; 2.80 A; A/B=39-764.
PDB; 2P8S; X-ray; 2.20 A; A/B=40-766.
PDB; 2QJR; X-ray; 2.20 A; A/B=31-766.
PDB; 2QKY; X-ray; 3.10 A; A/B/C/D=40-766.
PDB; 2QOE; X-ray; 2.30 A; A/B=39-766.
PDB; 2QT9; X-ray; 2.10 A; A/B=1-766.
PDB; 2QTB; X-ray; 2.25 A; A/B=1-766.
PDB; 2RGU; X-ray; 2.60 A; A/B=39-766.
PDB; 2RIP; X-ray; 2.90 A; A=38-766.
PDB; 3BJM; X-ray; 2.35 A; A/B=39-766.
PDB; 3C43; X-ray; 2.30 A; A/B=39-766.
PDB; 3C45; X-ray; 2.05 A; A/B=39-766.
PDB; 3CCB; X-ray; 2.49 A; A/B/C/D=39-766.
PDB; 3CCC; X-ray; 2.71 A; A/B/C/D=39-766.
PDB; 3D4L; X-ray; 2.00 A; A/B=39-766.
PDB; 3EIO; X-ray; 2.00 A; A/B=39-766.
PDB; 3F8S; X-ray; 2.43 A; A/B=31-766.
PDB; 3G0B; X-ray; 2.25 A; A/B/C/D=39-766.
PDB; 3G0C; X-ray; 2.69 A; A/B/C/D=39-766.
PDB; 3G0D; X-ray; 2.39 A; A/B/C/D=39-766.
PDB; 3G0G; X-ray; 2.45 A; A/B/C/D=39-766.
PDB; 3H0C; X-ray; 2.66 A; A/B=39-766.
PDB; 3HAB; X-ray; 2.10 A; A/B=39-766.
PDB; 3HAC; X-ray; 2.00 A; A/B=39-766.
PDB; 3KWF; X-ray; 2.40 A; A/B=39-766.
PDB; 3KWJ; X-ray; 2.80 A; A/B=39-766.
PDB; 3NOX; X-ray; 2.34 A; A/B=39-766.
PDB; 3O95; X-ray; 2.85 A; A/B/C/D=39-766.
PDB; 3O9V; X-ray; 2.75 A; A/B/C/D=39-766.
PDB; 3OC0; X-ray; 2.70 A; A/B=39-766.
PDB; 3OPM; X-ray; 2.72 A; A/B/C/D=39-766.
PDB; 3Q0T; X-ray; 2.40 A; A/B=39-766.
PDB; 3Q8W; X-ray; 3.64 A; A/B=39-764.
PDB; 3QBJ; X-ray; 2.21 A; A/B=31-766.
PDB; 3SWW; X-ray; 2.00 A; A/B=39-766.
PDB; 3SX4; X-ray; 2.60 A; A/B=39-766.
PDB; 3VJK; X-ray; 2.49 A; A/B=33-766.
PDB; 3VJL; X-ray; 2.39 A; A/B=33-766.
PDB; 3VJM; X-ray; 2.10 A; A/B=33-766.
PDB; 3W2T; X-ray; 2.36 A; A/B=33-766.
PDB; 3WQH; X-ray; 2.85 A; A/B=39-766.
PDB; 4A5S; X-ray; 1.62 A; A/B=39-766.
PDB; 4DSA; X-ray; 3.25 A; A/B=39-766.
PDB; 4DSZ; X-ray; 3.20 A; A/B=39-766.
PDB; 4DTC; X-ray; 3.00 A; A/B=39-766.
PDB; 4G1F; X-ray; 2.90 A; A/B/C/D=39-766.
PDB; 4J3J; X-ray; 3.20 A; A/B=39-766.
PDB; 4JH0; X-ray; 2.35 A; A/B=39-766.
PDB; 4KR0; X-ray; 2.70 A; A=39-766.
PDB; 4L72; X-ray; 3.00 A; A=39-766.
PDB; 4LKO; X-ray; 2.43 A; A/B=39-766.
PDB; 4N8D; X-ray; 1.65 A; A/B=39-766.
PDB; 4N8E; X-ray; 2.30 A; A/B=39-766.
PDB; 4PNZ; X-ray; 1.90 A; A/B=39-766.
PDB; 4PV7; X-ray; 3.24 A; A/B=39-766.
PDB; 4QZV; X-ray; 2.59 A; A/C=39-766.
PDB; 5I7U; X-ray; 1.95 A; A/B=39-766.
PDB; 5ISM; X-ray; 2.00 A; A/B=39-766.
PDB; 5J3J; X-ray; 2.75 A; A/B=40-766.
PDB; 5KBY; X-ray; 2.24 A; A/B/C/D=39-766.
PDB; 5T4B; X-ray; 1.76 A; A/B=40-766.
PDB; 5T4E; X-ray; 1.77 A; A/B=40-766.
PDB; 5T4F; X-ray; 1.90 A; A/B=40-766.
PDB; 5T4H; X-ray; 2.61 A; A/B=40-766.
PDBsum; 1J2E; -.
PDBsum; 1N1M; -.
PDBsum; 1NU6; -.
PDBsum; 1NU8; -.
PDBsum; 1PFQ; -.
PDBsum; 1R9M; -.
PDBsum; 1R9N; -.
PDBsum; 1RWQ; -.
PDBsum; 1TK3; -.
PDBsum; 1TKR; -.
PDBsum; 1U8E; -.
PDBsum; 1W1I; -.
PDBsum; 1WCY; -.
PDBsum; 1X70; -.
PDBsum; 2AJL; -.
PDBsum; 2BGN; -.
PDBsum; 2BGR; -.
PDBsum; 2BUB; -.
PDBsum; 2FJP; -.
PDBsum; 2G5P; -.
PDBsum; 2G5T; -.
PDBsum; 2G63; -.
PDBsum; 2HHA; -.
PDBsum; 2I03; -.
PDBsum; 2I78; -.
PDBsum; 2IIT; -.
PDBsum; 2IIV; -.
PDBsum; 2JID; -.
PDBsum; 2OAG; -.
PDBsum; 2OGZ; -.
PDBsum; 2OLE; -.
PDBsum; 2ONC; -.
PDBsum; 2OPH; -.
PDBsum; 2OQI; -.
PDBsum; 2OQV; -.
PDBsum; 2P8S; -.
PDBsum; 2QJR; -.
PDBsum; 2QKY; -.
PDBsum; 2QOE; -.
PDBsum; 2QT9; -.
PDBsum; 2QTB; -.
PDBsum; 2RGU; -.
PDBsum; 2RIP; -.
PDBsum; 3BJM; -.
PDBsum; 3C43; -.
PDBsum; 3C45; -.
PDBsum; 3CCB; -.
PDBsum; 3CCC; -.
PDBsum; 3D4L; -.
PDBsum; 3EIO; -.
PDBsum; 3F8S; -.
PDBsum; 3G0B; -.
PDBsum; 3G0C; -.
PDBsum; 3G0D; -.
PDBsum; 3G0G; -.
PDBsum; 3H0C; -.
PDBsum; 3HAB; -.
PDBsum; 3HAC; -.
PDBsum; 3KWF; -.
PDBsum; 3KWJ; -.
PDBsum; 3NOX; -.
PDBsum; 3O95; -.
PDBsum; 3O9V; -.
PDBsum; 3OC0; -.
PDBsum; 3OPM; -.
PDBsum; 3Q0T; -.
PDBsum; 3Q8W; -.
PDBsum; 3QBJ; -.
PDBsum; 3SWW; -.
PDBsum; 3SX4; -.
PDBsum; 3VJK; -.
PDBsum; 3VJL; -.
PDBsum; 3VJM; -.
PDBsum; 3W2T; -.
PDBsum; 3WQH; -.
PDBsum; 4A5S; -.
PDBsum; 4DSA; -.
PDBsum; 4DSZ; -.
PDBsum; 4DTC; -.
PDBsum; 4G1F; -.
PDBsum; 4J3J; -.
PDBsum; 4JH0; -.
PDBsum; 4KR0; -.
PDBsum; 4L72; -.
PDBsum; 4LKO; -.
PDBsum; 4N8D; -.
PDBsum; 4N8E; -.
PDBsum; 4PNZ; -.
PDBsum; 4PV7; -.
PDBsum; 4QZV; -.
PDBsum; 5I7U; -.
PDBsum; 5ISM; -.
PDBsum; 5J3J; -.
PDBsum; 5KBY; -.
PDBsum; 5T4B; -.
PDBsum; 5T4E; -.
PDBsum; 5T4F; -.
PDBsum; 5T4H; -.
ProteinModelPortal; P27487; -.
SMR; P27487; -.
BioGrid; 108137; 7.
DIP; DIP-351N; -.
IntAct; P27487; 21.
MINT; MINT-4998658; -.
STRING; 9606.ENSP00000353731; -.
BindingDB; P27487; -.
ChEMBL; CHEMBL284; -.
DrugBank; DB07482; (2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE.
DrugBank; DB03253; (2s)-Pyrrolidin-2-Ylmethylamine.
DrugBank; DB04577; 1-(1-phenylcyclopentyl)methylamine.
DrugBank; DB08024; 1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-2-(S)-CARBONITRILE.
DrugBank; DB07412; 1-biphenyl-2-ylmethanamine.
DrugBank; DB08588; 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-4-OXOQUINAZOLIN-3(4H)-YL}METHYL)BENZONITRILE.
DrugBank; DB01884; 2-Amino-3-Methyl-1-Pyrrolidin-1-Yl-Butan-1-One.
DrugBank; DB08672; 4-[(3R)-3-{[2-(4-FLUOROPHENYL)-2-OXOETHYL]AMINO}BUTYL]BENZAMIDE.
DrugBank; DB03660; 4-Iodo-L-phenylalanine.
DrugBank; DB07239; 7-(aminomethyl)-6-(2-chlorophenyl)-1-methyl-1H-benzimidazole-5-carbonitrile.
DrugBank; DB06203; Alogliptin.
DrugBank; DB01076; Atorvastatin.
DrugBank; DB04491; Diisopropylphosphono Group.
DrugBank; DB06127; KRP-104.
DrugBank; DB08882; Linagliptin.
DrugBank; DB06655; Liraglutide.
DrugBank; DB07779; N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE.
DrugBank; DB08429; N-({(2S)-1-[(3R)-3-amino-4-(3-chlorophenyl)butanoyl]pyrrolidin-2-yl}methyl)-3-(methylsulfonyl)benzamide.
DrugBank; DB05065; PHX1149.
DrugBank; DB05001; PSN9301.
DrugBank; DB06335; Saxagliptin.
DrugBank; DB01261; Sitagliptin.
DrugBank; DB04876; Vildagliptin.
GuidetoPHARMACOLOGY; 1612; -.
ESTHER; human-DPP4; DPP4N_Peptidase_S9.
MEROPS; S09.003; -.
iPTMnet; P27487; -.
PhosphoSitePlus; P27487; -.
BioMuta; DPP4; -.
DMDM; 1352311; -.
EPD; P27487; -.
MaxQB; P27487; -.
PaxDb; P27487; -.
PeptideAtlas; P27487; -.
PRIDE; P27487; -.
DNASU; 1803; -.
Ensembl; ENST00000360534; ENSP00000353731; ENSG00000197635.
GeneID; 1803; -.
KEGG; hsa:1803; -.
UCSC; uc002ubz.4; human.
CTD; 1803; -.
DisGeNET; 1803; -.
GeneCards; DPP4; -.
HGNC; HGNC:3009; DPP4.
HPA; CAB045970; -.
MIM; 102720; gene.
neXtProt; NX_P27487; -.
OpenTargets; ENSG00000197635; -.
PharmGKB; PA27467; -.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
GeneTree; ENSGT00760000119233; -.
HOGENOM; HOG000231875; -.
HOVERGEN; HBG005527; -.
InParanoid; P27487; -.
KO; K01278; -.
OMA; QFILLEY; -.
OrthoDB; EOG091G0BU5; -.
PhylomeDB; P27487; -.
TreeFam; TF313309; -.
BRENDA; 3.4.14.5; 2681.
Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
SABIO-RK; P27487; -.
SIGNOR; P27487; -.
ChiTaRS; DPP4; human.
EvolutionaryTrace; P27487; -.
GeneWiki; Dipeptidyl_peptidase-4; -.
GenomeRNAi; 1803; -.
PRO; PR:P27487; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000197635; -.
CleanEx; HS_DPP4; -.
ExpressionAtlas; P27487; baseline and differential.
Genevisible; P27487; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046581; C:intercellular canaliculus; IEA:Ensembl.
GO; GO:0071438; C:invadopodium membrane; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IDA:CACAO.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0043542; P:endothelial cell migration; IDA:UniProtKB.
GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0036343; P:psychomotor behavior; IEA:Ensembl.
GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002471; Pept_S9_AS.
InterPro; IPR001375; Peptidase_S9.
InterPro; IPR002469; Peptidase_S9B_N.
Pfam; PF00930; DPPIV_N; 1.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
1: Evidence at protein level;
3D-structure; Aminopeptidase; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Protease; Receptor; Reference proteome; Secreted;
Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 766 Dipeptidyl peptidase 4 membrane form.
/FTId=PRO_0000027213.
CHAIN 39 766 Dipeptidyl peptidase 4 soluble form.
/FTId=PRO_0000027214.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 766 Extracellular. {ECO:0000255}.
ACT_SITE 630 630 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 708 708 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 740 740 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:12646248,
ECO:0000269|PubMed:12906826,
ECO:0000269|PubMed:20684603}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20684603}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:12906826,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20684603}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:12646248,
ECO:0000269|PubMed:20684603}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:12646248,
ECO:0000269|PubMed:12906826,
ECO:0000269|PubMed:20684603}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:12646248,
ECO:0000269|PubMed:12906826}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:12646248}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12483204,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20684603}.
CARBOHYD 685 685 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
DISULFID 328 339
DISULFID 385 394
DISULFID 444 447
DISULFID 454 472
DISULFID 649 762
MUTAGEN 85 85 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 92 92 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 150 150 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 205 205 E->K: Inhibits dipeptidyl peptidase
activity. {ECO:0000269|PubMed:10570924}.
MUTAGEN 206 206 E->L: Inhibits dipeptidyl peptidase
activity. {ECO:0000269|PubMed:10570924}.
MUTAGEN 219 219 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 229 229 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 281 281 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 321 321 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 520 520 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 685 685 N->A: Does not inhibit dipeptidyl
peptidase activity, interaction with ADA
and homodimer formation.
{ECO:0000269|PubMed:14691230}.
MUTAGEN 750 750 H->A: Inhibits weakly homodimerization
and dipeptidyl peptidase activity.
{ECO:0000269|PubMed:15448155,
ECO:0000269|PubMed:17287217}.
MUTAGEN 750 750 H->E: Inhibits strongly homodimerization,
dipeptidyl peptidase activity,
interaction with CARD11 and T-cell
costimulation activity.
{ECO:0000269|PubMed:15448155,
ECO:0000269|PubMed:17287217}.
CONFLICT 6 6 K -> R (in Ref. 2; AAA52308).
{ECO:0000305}.
CONFLICT 7 7 V -> I (in Ref. 1; CAA43118).
{ECO:0000305}.
CONFLICT 437 437 S -> I (in Ref. 1; CAA43118).
{ECO:0000305}.
CONFLICT 557 557 T -> I (in Ref. 2; AAA52308).
{ECO:0000305}.
CONFLICT 663 663 D -> E (in Ref. 2; AAA52308).
{ECO:0000305}.
STRAND 40 42 {ECO:0000244|PDB:3VJM}.
HELIX 45 50 {ECO:0000244|PDB:4A5S}.
STRAND 60 62 {ECO:0000244|PDB:4A5S}.
STRAND 64 72 {ECO:0000244|PDB:4A5S}.
STRAND 75 80 {ECO:0000244|PDB:4A5S}.
TURN 81 83 {ECO:0000244|PDB:4A5S}.
STRAND 86 90 {ECO:0000244|PDB:4A5S}.
TURN 92 97 {ECO:0000244|PDB:4A5S}.
STRAND 98 100 {ECO:0000244|PDB:5T4B}.
STRAND 104 107 {ECO:0000244|PDB:4A5S}.
STRAND 111 122 {ECO:0000244|PDB:4A5S}.
STRAND 124 126 {ECO:0000244|PDB:4A5S}.
STRAND 128 136 {ECO:0000244|PDB:4A5S}.
TURN 137 140 {ECO:0000244|PDB:4A5S}.
STRAND 141 143 {ECO:0000244|PDB:3F8S}.
STRAND 152 157 {ECO:0000244|PDB:4A5S}.
STRAND 159 162 {ECO:0000244|PDB:4A5S}.
STRAND 164 168 {ECO:0000244|PDB:4A5S}.
STRAND 171 177 {ECO:0000244|PDB:4A5S}.
TURN 191 193 {ECO:0000244|PDB:4A5S}.
STRAND 194 198 {ECO:0000244|PDB:4A5S}.
HELIX 201 206 {ECO:0000244|PDB:4A5S}.
STRAND 208 212 {ECO:0000244|PDB:4A5S}.
STRAND 214 216 {ECO:0000244|PDB:4A5S}.
STRAND 220 229 {ECO:0000244|PDB:4A5S}.
STRAND 235 240 {ECO:0000244|PDB:4A5S}.
STRAND 250 255 {ECO:0000244|PDB:4A5S}.
STRAND 265 272 {ECO:0000244|PDB:4A5S}.
HELIX 273 275 {ECO:0000244|PDB:4N8D}.
STRAND 278 280 {ECO:0000244|PDB:4A5S}.
STRAND 284 287 {ECO:0000244|PDB:4A5S}.
HELIX 291 294 {ECO:0000244|PDB:4A5S}.
STRAND 298 307 {ECO:0000244|PDB:4A5S}.
STRAND 310 319 {ECO:0000244|PDB:4A5S}.
STRAND 322 330 {ECO:0000244|PDB:4A5S}.
TURN 332 334 {ECO:0000244|PDB:4A5S}.
STRAND 337 339 {ECO:0000244|PDB:4A5S}.
HELIX 341 343 {ECO:0000244|PDB:4A5S}.
STRAND 345 348 {ECO:0000244|PDB:4A5S}.
STRAND 350 352 {ECO:0000244|PDB:4A5S}.
STRAND 354 358 {ECO:0000244|PDB:4A5S}.
STRAND 362 364 {ECO:0000244|PDB:1NU8}.
STRAND 368 376 {ECO:0000244|PDB:4A5S}.
STRAND 378 380 {ECO:0000244|PDB:2G5P}.
STRAND 382 388 {ECO:0000244|PDB:4A5S}.
STRAND 391 393 {ECO:0000244|PDB:3SWW}.
STRAND 395 397 {ECO:0000244|PDB:4A5S}.
STRAND 400 402 {ECO:0000244|PDB:4A5S}.
STRAND 404 410 {ECO:0000244|PDB:4A5S}.
STRAND 412 420 {ECO:0000244|PDB:4A5S}.
HELIX 422 424 {ECO:0000244|PDB:4A5S}.
STRAND 429 435 {ECO:0000244|PDB:4A5S}.
STRAND 438 446 {ECO:0000244|PDB:4A5S}.
TURN 447 449 {ECO:0000244|PDB:1PFQ}.
TURN 451 453 {ECO:0000244|PDB:4A5S}.
STRAND 456 461 {ECO:0000244|PDB:4A5S}.
STRAND 465 472 {ECO:0000244|PDB:4A5S}.
STRAND 474 477 {ECO:0000244|PDB:4A5S}.
STRAND 479 484 {ECO:0000244|PDB:4A5S}.
TURN 485 488 {ECO:0000244|PDB:4A5S}.
STRAND 489 495 {ECO:0000244|PDB:4A5S}.
HELIX 498 504 {ECO:0000244|PDB:4A5S}.
STRAND 506 508 {ECO:0000244|PDB:3G0B}.
STRAND 511 519 {ECO:0000244|PDB:4A5S}.
STRAND 522 530 {ECO:0000244|PDB:4A5S}.
STRAND 536 538 {ECO:0000244|PDB:1PFQ}.
STRAND 540 545 {ECO:0000244|PDB:4A5S}.
HELIX 563 569 {ECO:0000244|PDB:4A5S}.
STRAND 574 578 {ECO:0000244|PDB:4A5S}.
STRAND 584 586 {ECO:0000244|PDB:4A5S}.
HELIX 588 591 {ECO:0000244|PDB:4A5S}.
HELIX 592 594 {ECO:0000244|PDB:4A5S}.
TURN 598 600 {ECO:0000244|PDB:3H0C}.
HELIX 601 614 {ECO:0000244|PDB:4A5S}.
TURN 615 617 {ECO:0000244|PDB:3VJK}.
STRAND 619 629 {ECO:0000244|PDB:4A5S}.
HELIX 631 640 {ECO:0000244|PDB:4A5S}.
TURN 641 643 {ECO:0000244|PDB:4A5S}.
STRAND 648 654 {ECO:0000244|PDB:4A5S}.
HELIX 659 661 {ECO:0000244|PDB:4A5S}.
HELIX 664 671 {ECO:0000244|PDB:4A5S}.
TURN 676 679 {ECO:0000244|PDB:4A5S}.
HELIX 680 685 {ECO:0000244|PDB:4A5S}.
HELIX 689 697 {ECO:0000244|PDB:4A5S}.
STRAND 698 705 {ECO:0000244|PDB:4A5S}.
STRAND 709 711 {ECO:0000244|PDB:4A5S}.
HELIX 714 725 {ECO:0000244|PDB:4A5S}.
STRAND 731 735 {ECO:0000244|PDB:4A5S}.
HELIX 745 762 {ECO:0000244|PDB:4A5S}.
SEQUENCE 766 AA; 88279 MW; 5FB4A2C6662D6117 CRC64;
MKTPWKVLLG LLGAAALVTI ITVPVVLLNK GTDDATADSR KTYTLTDYLK NTYRLKLYSL
RWISDHEYLY KQENNILVFN AEYGNSSVFL ENSTFDEFGH SINDYSISPD GQFILLEYNY
VKQWRHSYTA SYDIYDLNKR QLITEERIPN NTQWVTWSPV GHKLAYVWNN DIYVKIEPNL
PSYRITWTGK EDIIYNGITD WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF
YSDESLQYPK TVRVPYPKAG AVNPTVKFFV VNTDSLSSVT NATSIQITAP ASMLIGDHYL
CDVTWATQER ISLQWLRRIQ NYSVMDICDY DESSGRWNCL VARQHIEMST TGWVGRFRPS
EPHFTLDGNS FYKIISNEEG YRHICYFQID KKDCTFITKG TWEVIGIEAL TSDYLYYISN
EYKGMPGGRN LYKIQLSDYT KVTCLSCELN PERCQYYSVS FSKEAKYYQL RCSGPGLPLY
TLHSSVNDKG LRVLEDNSAL DKMLQNVQMP SKKLDFIILN ETKFWYQMIL PPHFDKSKKY
PLLLDVYAGP CSQKADTVFR LNWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT
FEVEDQIEAA RQFSKMGFVD NKRIAIWGWS YGGYVTSMVL GSGSGVFKCG IAVAPVSRWE
YYDSVYTERY MGLPTPEDNL DHYRNSTVMS RAENFKQVEY LLIHGTADDN VHFQQSAQIS
KALVDVGVDF QAMWYTDEDH GIASSTAHQH IYTHMSHFIK QCFSLP


Related products :

Catalog number Product name Quantity
U0884h CLIA ADABP,ADCP2,ADCP-2,Adenosine deaminase complexing protein 2,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Homo sapiens,Human,T-cell activation antigen CD26,TP103 96T
E0884h ELISA kit ADABP,ADCP2,ADCP-2,Adenosine deaminase complexing protein 2,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Homo sapiens,Human,T-cell activation antigen CD26,TP103 96T
E0884h ELISA ADABP,ADCP2,ADCP-2,Adenosine deaminase complexing protein 2,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Homo sapiens,Human,T-cell activation antigen CD26,TP103 96T
15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.1 mg
15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.05 mg
E0884b ELISA kit ACT3,Activation molecule 3,ADCP-I,Adenosine deaminase complexing protein,Bos taurus,Bovine,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,T-cell activation antigen CD26,WC1 96T
U0884b CLIA ACT3,Activation molecule 3,ADCP-I,Adenosine deaminase complexing protein,Bos taurus,Bovine,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,T-cell activation antigen CD26,WC10 96T
E0884b ELISA ACT3,Activation molecule 3,ADCP-I,Adenosine deaminase complexing protein,Bos taurus,Bovine,CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,T-cell activation antigen CD26,WC10 96T
20-321-175240 DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26 - MONOCLONAL ANTIBODY TO RAT DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26; EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosi 0.1 mg
EIAAB11842 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,DPP2,DPP7,Homo sapiens,Human,QPP,Quiescent cell proline dipeptidase
EIAAB11839 Dipeptidyl peptidase IV-related protein 3,Dipeptidyl peptidase X,Dipeptidyl peptidase-like protein 2,DPL2,DPP X,DPP10,DPRP3,DPRP-3,Homo sapiens,Human,Inactive dipeptidyl peptidase 10,KIAA1492
EIAAB11843 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Quiescent cell proline dipeptidase,Rat,Rattus norvegicus
EIAAB11844 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Mouse,Mus musculus,Qpp,Quiescent cell proline dipeptidase
E0884r ELISA Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD26 96T
U0884r CLIA Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD26 96T
EIAAB11854 Dipeptidyl peptidase 9,Dipeptidyl peptidase IV-related protein 2,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,DPP9,DPRP2,DPRP-2,Homo sapiens,Human
E0884m ELISA kit Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,Mouse,Mus musculus,T-cell activation antigen CD26,THAM,Thymocyte-activating molecule 96T
U0884m CLIA Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,Mouse,Mus musculus,T-cell activation antigen CD26,THAM,Thymocyte-activating molecule 96T
E0884m ELISA Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,Mouse,Mus musculus,T-cell activation antigen CD26,THAM,Thymocyte-activating molecule 96T
E0884r ELISA kit Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD2 96T
E0884p ELISA kit CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Pig,Sus scrofa,T-cell activation antigen CD26 96T
E0884p ELISA CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Pig,Sus scrofa,T-cell activation antigen CD26 96T
U0884p CLIA CD26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,DPP4,Pig,Sus scrofa,T-cell activation antigen CD26 96T
EIAAB11845 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,DPP3,Homo sapiens,Human
EIAAB11855 Dipeptidyl peptidase 9,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,Dpp9,Mouse,Mus musculus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur